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Volumn 9, Issue 13, 1999, Pages 715-718

Aromatic and basic residues within the EVH1 domain of VASP specify its interaction with proline-rich ligands

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); ENA; LISTERIA MONOCYTOGENES; MENA; MURINAE;

EID: 0033166687     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80315-7     Document Type: Article
Times cited : (73)

References (11)
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  • 5
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  • 6
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    • A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
    • Niebuhr K, Ebel F, Frank R, Reinhard R, Domann E, Carl UD, et al.: A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. EMBO J 1997, 16:5433-5444.
    • (1997) EMBO J , vol.16 , pp. 5433-5444
    • Niebuhr, K.1    Ebel, F.2    Frank, R.3    Reinhard, R.4    Domann, E.5    Carl, U.D.6
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    • Structural basis for the binding of proline-rich peptides to SH3 domains
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.